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Q8L7Q7 (PME64_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable pectinesterase/pectinesterase inhibitor 64

Including the following 2 domains:

  1. Pectinesterase inhibitor 64
    Alternative name(s):
    Pectin methylesterase inhibitor 64
  2. Pectinesterase 64
    Short name=PE 64
    EC=3.1.1.11
    Alternative name(s):
    Pectin methylesterase 64
    Short name=AtPME64
Gene names
Name:PME64
Synonyms:ARATH64
Ordered Locus Names:At5g64640
ORF Names:MUB3.16
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acts in the modification of cell walls via demethylesterification of cell wall pectin By similarity.

Catalytic activity

Pectin + n H2O = n methanol + pectate.

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in siliques. Ref.5

Developmental stage

Expressed during late developmental phases of siliques. Ref.5

Miscellaneous

The PMEI region may act as an autoinhibitory domain and prevent untimely PME activity during transport.

Sequence similarities

In the N-terminal section; belongs to the PMEI family.

In the C-terminal section; belongs to the pectinesterase family.

Sequence caution

The sequence AAM91523.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 602602Probable pectinesterase/pectinesterase inhibitor 64
PRO_0000371709

Regions

Transmembrane36 – 5621Helical; Potential
Region87 – 237151Pectinesterase inhibitor 64
Region288 – 595308Pectinesterase 64
Compositional bias68 – 12255Pro-rich

Sites

Active site4201Proton donor; for pectinesterase activity By similarity
Active site4411Nucleophile; for pectinesterase activity By similarity
Binding site3671Substrate; for pectinesterase activity By similarity
Binding site3971Substrate; for pectinesterase activity By similarity
Binding site5181Substrate; for pectinesterase activity By similarity
Binding site5201Substrate; for pectinesterase activity By similarity
Site4191Transition state stabilizer By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2291N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation4961N-linked (GlcNAc...) Potential
Disulfide bond434 ↔ 454 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8L7Q7 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 1667501044317054

FASTA60265,478
        10         20         30         40         50         60 
MDSPTLPHSI SASSSTPFAS AAVKPHRNKL LSRNGILIII AASCILLLLI SLLIYATVSK 

        70         80         90        100        110        120 
SSRNHHNPSH QTPTSDDHPP PETPPSPPPI AQIRLACNAT RFPDHCVASL SKPGQVPPDP 

       130        140        150        160        170        180 
KPVQIIHSAI SVSYENLKSG QSKIQSILDS SAGNRNRTNI ATICLEILSY SQHRTESTDI 

       190        200        210        220        230        240 
AVTSGDIKDA RAWMSAALAY QFDCWSGLKT VNDTKQVVDT ITFFEGLVNL TGNALSMMLS 

       250        260        270        280        290        300 
FDSFGDDVVS WIRPATERDG FWEKAGPSLG SGTGTEASLG FPSGLTEDVT VCKNGGKDCK 

       310        320        330        340        350        360 
YKTVQEAVDS APDTNRTVKF VIRIREGVYE ETVRVPFEKK NVVFIGDGMG KTVITGSLNV 

       370        380        390        400        410        420 
GQPGMTTFES ATVGVLGDGF MARDLTIENT AGADAHQAVA FRSDSDFSVL ENCEFLGNQD 

       430        440        450        460        470        480 
TLYAHSLRQF YKQCRIQGNV DFIFGNSAAV FQDCDILIAS KHSKLEQGGA NNAITAHGRI 

       490        500        510        520        530        540 
DASQSTGFVF LNCSINGTEE YMKEFQANPE GHKNFLGRPW KEFSRTVFVN CNLESLISPD 

       550        560        570        580        590        600 
GWMPWNGDFA LKTLYYGEYK NTGPGSVRSS RVPWSSEIPE KHVDVYSVAN FIQADEWAST 


TA

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:41-54(1998) [PubMed: 9628582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-602.
Strain: cv. Columbia.
[4]"Pectin methylesterases: sequence-structural features and phylogenetic relationships."
Markovic O., Janecek S.
Carbohydr. Res. 339:2281-2295(2004) [PubMed: 15337457] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[5]"Comprehensive expression profiling of the pectin methylesterase gene family during silique development in Arabidopsis thaliana."
Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F., Guerineau F., Pelloux J.
Planta 224:782-791(2006) [PubMed: 16622707] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB010076 Genomic DNA. Translation: BAB11431.1.
CP002688 Genomic DNA. Translation: AED97931.1.
AY128320 mRNA. Translation: AAM91523.1. Different initiation.
IPIIPI00529671.
RefSeqNP_568991.2. NM_125860.4.
UniGeneAt.28947.
At.69346.

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ProteinModelPortalQ8L7Q7.
SMRQ8L7Q7. Positions 282-602.
ModBaseSearch...

Proteomic databases

PRIDEQ8L7Q7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G64640.1; AT5G64640.1; AT5G64640.
GeneID836585.
GenomeReviewsGene locus AT5G64640 in contig BA000015_GR.
KEGGath:AT5G64640.

Organism-specific databases

GeneFarm224. 8.
TAIRAt5g64640.

Phylogenomic databases

eggNOGCOG4677.
OMAACNATRF.
PhylomeDBQ8L7Q7.
ProtClustDBPLN02708.

Enzyme and pathway databases

BRENDA3.1.1.11. 399.

Gene expression databases

ArrayExpressQ8L7Q7.
GenevestigatorQ8L7Q7.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR000070. Pectinesterase_cat.
IPR006501. Pectinesterase_inhib.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
G3DSA:1.20.140.40. Pectinesterase_inhib. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
PF04043. PMEI. 1 hit.
[Graphical view]
SMARTSM00856. PMEI. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
SSF101148. Pectinesterase_inhib. 1 hit.
TIGRFAMsTIGR01614. PME_inhib. 1 hit.
PROSITEPS00800. PECTINESTERASE_1. False negative.
PS00503. PECTINESTERASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME64_ARATH
AccessionPrimary (citable) accession number: Q8L7Q7
Secondary accession number(s): Q9FLF6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: September 21, 2011
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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